FSIP1 binds HER2 directly to regulate breast cancer growth and invasiveness

Liu, Tong; Zhang, Hao; Sun, Li; Zhao, Danyu; Liu, Peng; Yan, Meisi; Zaidi, Neeha; Izadmehr, Sudeh; Gupta, Animesh; Abu‐Amer, Wahid; Luo, Min; Yang, Jie; Ou, Xunyan; Wang, Yining; Bai, Xuefeng; Wang, Yan; New, Maria I.; Zaidi, Mone; Yuen, Tony; Liu, Caigang

doi:10.1073/pnas.1621486114

Cited by 26 publications

(27 citation statements)

References 22 publications

(39 reference statements)

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“…The microscale thermophoresis assay was performed as previously described, with minor modifications (42, 43). Recombinant cMCR‐1 was labeled using the Monolith NT protein labeling kit RED (L001; NanoTemper Technologies, Munich, Germany) according to the manufacturer's protocol.…”

Section: Methodsmentioning

confidence: 99%

Substrate analog interaction with MCR‐1 offers insight into the rising threat of the plasmid‐mediated transferable colistin resistance

et al. 2018

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Colistin is considered a last-resort antibiotic against most gram-negative bacteria. Recent discoveries of a plasmid-mediated, transferable mobilized colistin-resistance gene ( mcr-1) on all continents have heralded the imminent emergence of pan-drug-resistant superbacteria. The inner-membrane protein MCR-1 can catalyze the transfer of phosphoethanolamine (PEA) to lipid A, resulting in colistin resistance. However, little is known about the mechanism, and few drugs exist to address this issue. We present crystal structures revealing the MCR-1 catalytic domain (cMCR-1) as a monozinc metalloprotein with ethanolamine (ETA) and d-glucose, respectively, thus highlighting 2 possible substrate-binding pockets in the MCR-1-catalyzed PEA transfer reaction. Mutation of the residues involved in ETA and d-glucose binding impairs colistin resistance in recombinant Escherichia coli containing full-length MCR-1. Partial analogs of the substrate are used for cocrystallization with cMCR-1, providing valuable information about the family of PEA transferases. One of the analogs, ETA, causes clear inhibition of polymyxin B resistance, highlighting its potential for drug development. These data demonstrate the crucial role of the PEA- and lipid A-binding pockets and provide novel insights into the structure-based mechanisms, important drug-target hot spots, and a drug template for further drug development to combat the urgent, rising threat of MCR-1-mediated antibiotic resistance.-Wei, P., Song, G., Shi, M., Zhou, Y., Liu, Y., Lei, J., Chen, P., Yin, L. Substrate analog interaction with MCR-1 offers insight into the rising threat of the plasmid-mediated transferable colistin resistance.

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Section: Methodsmentioning

confidence: 99%

Substrate analog interaction with MCR‐1 offers insight into the rising threat of the plasmid‐mediated transferable colistin resistance

et al. 2018

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“…The impact of EDNRB silencing on the migration of breast cancer cells was determined by the Transwell migration assay . Briefly, MDA‐MB‐231/EDNRBsh, control MDA‐MB‐231/NC, BT549/EDNRBsh, and control BT549/NC cells (2 × 10 4 cells/well) were loaded into the upper chamber of 24‐well Transwell plates (8 µm pore size; Corning) in FBS‐free medium.…”

Section: Methodsmentioning

confidence: 99%

Knockdown of endothelin receptor B inhibits the progression of triple‐negative breast cancer

Han

Cui

et al. 2019

Annals of the New York Academy of Sciences

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Endothelin receptor B (EDNRB) is one of the receptors in the endothelin axis and its upregulated expression is associated with tumorigenesis and metastasis of several types of solid tumors. However, the expression profile of EDNRB in breast cancer and its role in the progression of breast cancer are unclear. Here, we show that EDNRB expression is higher in metastatic tumors than in primary breast cancer, and is associated significantly with lymph node metastasis and poor survival in Chinese patients with breast cancer. EDNRB expression was particularly upregulated in triple‐negative breast cancer (TNBC) cells. Moreover, EDNRB silencing by a specific shRNA significantly attenuated the proliferation, migration, and invasiveness of MDA‐MB‐231 and BT549 cells and increased their apoptosis, as well as retarded the growth of implanted tumors in mice. Tandem mass spectrometry analysis indicated that 248 proteins were differentially expressed in EDNRB‐silenced cells and their cellular organelles, and these proteins participate in many processes. EDNRB silencing decreased protein kinase B and extracellular regulated protein kinase phosphorylation and promoted the mesenchymal‐to‐epithelial transition process in MDA‐MB‐231 cells. Therefore, our findings provide strong evidence for the first time that knockdown of EDNRB expression inhibits the progression of TNBC and that EDNRB can serve as a prognostic biomarker and therapeutic target for the treatment of TNBC.

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“…Moreover, VDAC1-based peptides were synthesized to act as a targeted drug in suppression antiapoptotic activity of Bcl-xL protein. Similarly, Liu et al [41] used MST to investigate direct interaction of fibrous sheath interacting protein 1 (FSIP1) to human epidermal growth factor receptor 2 (HER2). Where, FSIP1 is a known biomarker correlate to HER2 in growth and metastasis of breast cancer.…”

Section: Protein-protein Interactionsmentioning

confidence: 99%

Thermophoresis for characterizing biomolecular interaction

Asmari

Ratih

Alhazmi

et al. 2018

Methods

100

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The study of biomolecular interactions is crucial to get more insight into the biological system. The interactions of protein-protein, protein-nucleic acids, protein-sugars, nucleic acid-nucleic acids and protein-small molecules are supporting therapeutics and technological developments. Recently, the development in a large number of analytical techniques for characterizing biomolecular interactions reflect the promising research investments in this field. In this review, microscale thermophoresis technology (MST) is presented as an analytical technique for characterizing biomolecular interactions. Recent years have seen much progress and several applications established. MST is a powerful technique in quantitation of binding events based on the movement of molecules in microscopic temperature gradient. Simplicity, free solutions analysis, low sample volume, short analysis time, and immobilization free are the MST advantages over other competitive techniques. A wide range of studies in biomolecular interactions have been successfully carried out using MST, which tend to the versatility of the technique to use in screening binding events in order to save time, cost and obtained high data quality.

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FSIP1 binds HER2 directly to regulate breast cancer growth and invasiveness

Cited by 26 publications

References 22 publications

Substrate analog interaction with MCR‐1 offers insight into the rising threat of the plasmid‐mediated transferable colistin resistance

Substrate analog interaction with MCR‐1 offers insight into the rising threat of the plasmid‐mediated transferable colistin resistance

Knockdown of endothelin receptor B inhibits the progression of triple‐negative breast cancer

Thermophoresis for characterizing biomolecular interaction

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